The bacterial chromosome: architecture and action of bacterial SMC and SMC-like complexes

Abstract Structural Maintenance of Chromosomes (SMC) protein complexes are found in all three domains of life. They are characterized by a distinctive and conserved architecture in which a globular ATPase ‘head’ domain is formed by the N- and C-terminal regions of the SMC protein coming together, wi...

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Published inFEMS microbiology reviews Vol. 38; no. 3; pp. 380 - 392
Main Authors Nolivos, Sophie, Sherratt, David
Format Journal Article
LanguageEnglish
Published Oxford, UK Blackwell Publishing Ltd 01.05.2014
Oxford University Press
Wiley-Blackwell
Subjects
Architecture
Bacteria
Bacterial Proteins - chemistry
Bacterial Proteins - metabolism
chromosome
chromosome organization
chromosome segregation
Chromosomes
Chromosomes, Bacterial - chemistry
Chromosomes, Bacterial - metabolism
cohesin
condensin
Life Sciences
Other
Review
SMC
SMC
condensin
cohesin
chromosome organization
chromosome segregation
chromosome
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Abstract Abstract Structural Maintenance of Chromosomes (SMC) protein complexes are found in all three domains of life. They are characterized by a distinctive and conserved architecture in which a globular ATPase ‘head’ domain is formed by the N- and C-terminal regions of the SMC protein coming together, with a c. 50-nm-long antiparallel coiled-coil separating the head from a dimerization ‘hinge’. Dimerization gives both V- and O-shaped SMC dimers. The distinctive architecture points to a conserved biochemical mechanism of action. However, the details of this mechanism are incomplete, and the precise ways in which this mechanism leads to the biological functions of these complexes in chromosome organization and processing remain unclear. In this review, we introduce the properties of bacterial SMC complexes, compare them with eukaryotic complexes and discuss how their likely biochemical action relates to their roles in chromosome organization and segregation. By reviewing the properties of SMC complexes in all three domains of life, we assess their likely common biochemical mechanism of action and propose how this might relate to the functions of bacterial SMC complexes in chromosome segregation and chromosome organization. By reviewing the properties of SMC complexes in all three domains of life, we assess their likely common biochemical mechanism of action and propose how this might relate to the functions of bacterial SMC complexes in chromosome segregation and chromosome organization.
AbstractList Structural Maintenance of Chromosomes (SMC) protein complexes are found in all three domains of life. They are characterized by a distinctive and conserved architecture in which a globular ATPase ‘head’ domain is formed by the N‐ and C‐terminal regions of the SMC protein coming together, with a c. 50‐nm‐long antiparallel coiled‐coil separating the head from a dimerization ‘hinge’. Dimerization gives both V‐ and O‐shaped SMC dimers. The distinctive architecture points to a conserved biochemical mechanism of action. However, the details of this mechanism are incomplete, and the precise ways in which this mechanism leads to the biological functions of these complexes in chromosome organization and processing remain unclear. In this review, we introduce the properties of bacterial SMC complexes, compare them with eukaryotic complexes and discuss how their likely biochemical action relates to their roles in chromosome organization and segregation. By reviewing the properties of SMC complexes in all three domains of life, we assess their likely common biochemical mechanism of action and propose how this might relate to the functions of bacterial SMC complexes in chromosome segregation and chromosome organization.
Structural Maintenance of Chromosomes (SMC) protein complexes are found in all three domains of life. They are characterized by a distinctive and conserved architecture in which a globular ATPase 'head' domain is formed by the N- and C-terminal regions of the SMC protein coming together, with a c. 50-nm-long antiparallel coiled-coil separating the head from a dimerization 'hinge'. Dimerization gives both V- and O-shaped SMC dimers. The distinctive architecture points to a conserved biochemical mechanism of action. However, the details of this mechanism are incomplete, and the precise ways in which this mechanism leads to the biological functions of these complexes in chromosome organization and processing remain unclear. In this review, we introduce the properties of bacterial SMC complexes, compare them with eukaryotic complexes and discuss how their likely biochemical action relates to their roles in chromosome organization and segregation.
Structural Maintenance of Chromosomes (SMC) protein complexes are found in all three domains of life. They are characterized by a distinctive and conserved architecture in which a globular ATPase 'head' domain is formed by the N- and C-terminal regions of the SMC protein coming together, with a c. 50-nm-long antiparallel coiled-coil separating the head from a dimerization 'hinge'. Dimerization gives both V- and O-shaped SMC dimers. The distinctive architecture points to a conserved biochemical mechanism of action. However, the details of this mechanism are incomplete, and the precise ways in which this mechanism leads to the biological functions of these complexes in chromosome organization and processing remain unclear. In this review, we introduce the properties of bacterial SMC complexes, compare them with eukaryotic complexes and discuss how their likely biochemical action relates to their roles in chromosome organization and segregation. By reviewing the properties of SMC complexes in all three domains of life, we assess their likely common biochemical mechanism of action and propose how this might relate to the functions of bacterial SMC complexes in chromosome segregation and chromosome organization.
Structural Maintenance of Chromosomes (SMC) protein complexes are found in all three domains of life. They are characterized by a distinctive and conserved architecture in which a globular ATPase 'head' domain is formed by the N- and C-terminal regions of the SMC protein coming together, with a c. 50-nm-long antiparallel coiled-coil separating the head from a dimerization 'hinge'. Dimerization gives both V- and O-shaped SMC dimers. The distinctive architecture points to a conserved biochemical mechanism of action. However, the details of this mechanism are incomplete, and the precise ways in which this mechanism leads to the biological functions of these complexes in chromosome organization and processing remain unclear. In this review, we introduce the properties of bacterial SMC complexes, compare them with eukaryotic complexes and discuss how their likely biochemical action relates to their roles in chromosome organization and segregation. [PUBLICATION ABSTRACT]
Abstract Structural Maintenance of Chromosomes (SMC) protein complexes are found in all three domains of life. They are characterized by a distinctive and conserved architecture in which a globular ATPase ‘head’ domain is formed by the N- and C-terminal regions of the SMC protein coming together, with a c. 50-nm-long antiparallel coiled-coil separating the head from a dimerization ‘hinge’. Dimerization gives both V- and O-shaped SMC dimers. The distinctive architecture points to a conserved biochemical mechanism of action. However, the details of this mechanism are incomplete, and the precise ways in which this mechanism leads to the biological functions of these complexes in chromosome organization and processing remain unclear. In this review, we introduce the properties of bacterial SMC complexes, compare them with eukaryotic complexes and discuss how their likely biochemical action relates to their roles in chromosome organization and segregation. By reviewing the properties of SMC complexes in all three domains of life, we assess their likely common biochemical mechanism of action and propose how this might relate to the functions of bacterial SMC complexes in chromosome segregation and chromosome organization. By reviewing the properties of SMC complexes in all three domains of life, we assess their likely common biochemical mechanism of action and propose how this might relate to the functions of bacterial SMC complexes in chromosome segregation and chromosome organization.
Structural Maintenance of Chromosomes (SMC) protein complexes are found in all three domains of life. They are characterized by a distinctive and conserved architecture in which a globular ATPase ‘head’ domain is formed by the N- and C-terminal regions of the SMC protein coming together, with a c . 50-nm-long antiparallel coiled-coil separating the head from a dimerization ‘hinge’. Dimerization gives both V- and O-shaped SMC dimers. The distinctive architecture points to a conserved biochemical mechanism of action. However, the details of this mechanism are incomplete, and the precise ways in which this mechanism leads to the biological functions of these complexes in chromosome organization and processing remain unclear. In this review, we introduce the properties of bacterial SMC complexes, compare them with eukaryotic complexes and discuss how their likely biochemical action relates to their roles in chromosome organization and segregation.
Author Sherratt, David
Nolivos, Sophie
Author_xml – sequence: 1
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  fullname: Nolivos, Sophie
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  surname: Sherratt
  fullname: Sherratt, David
  email: david.sherratt@bioch.ox.ac.uk
  organization: Department of Biochemistry, University of Oxford, Oxford, UK
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https://hal.science/hal-01893655$$DView record in HAL
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ContentType Journal Article
Copyright 2014 Federation of European Microbiological Societies. Published by John Wiley & Sons Ltd. All rights reserved 2014
2013 The Authors. FEMS Microbiology Reviews published by John Wiley & Sons Ltd on behalf of the Federation of European Microbiological Societies.
Copyright © 2014 Federation of European Microbiological Societies. Published by John Wiley & Sons Ltd. All rights reserved
Distributed under a Creative Commons Attribution 4.0 International License
2013 The Authors. FEMS Microbiology Reviews published by John Wiley & Sons Ltd on behalf of the Federation of European Microbiological Societies. 2013
Copyright_xml – notice: 2014 Federation of European Microbiological Societies. Published by John Wiley & Sons Ltd. All rights reserved 2014
– notice: 2013 The Authors. FEMS Microbiology Reviews published by John Wiley & Sons Ltd on behalf of the Federation of European Microbiological Societies.
– notice: Copyright © 2014 Federation of European Microbiological Societies. Published by John Wiley & Sons Ltd. All rights reserved
– notice: Distributed under a Creative Commons Attribution 4.0 International License
– notice: 2013 The Authors. FEMS Microbiology Reviews published by John Wiley & Sons Ltd on behalf of the Federation of European Microbiological Societies. 2013
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IEDL.DBID 24P
ISSN 0168-6445
1574-6976
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IsDoiOpenAccess true
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Issue 3
Keywords SMC
condensin
cohesin
chromosome organization
chromosome segregation
chromosome
Language English
License This is an Open Access article distributed under the terms of the Creative Commons Attribution-NonCommercial-NoDerivs licence (http://creativecommons.org/licenses/by-nc-nd/3.0/) which permits non-commercial reproduction and distribution of the work, in any medium, provided the original work is not altered or transformed in any way, and that the work is properly cited. For commercial re-use, please contact journals.permissions@oup.com
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Snippet Abstract Structural Maintenance of Chromosomes (SMC) protein complexes are found in all three domains of life. They are characterized by a distinctive and...
Structural Maintenance of Chromosomes (SMC) protein complexes are found in all three domains of life. They are characterized by a distinctive and conserved...
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SubjectTerms Architecture
Bacteria
Bacterial Proteins - chemistry
Bacterial Proteins - metabolism
chromosome
chromosome organization
chromosome segregation
Chromosomes
Chromosomes, Bacterial - chemistry
Chromosomes, Bacterial - metabolism
cohesin
condensin
Life Sciences
Other
Review
SMC
Title The bacterial chromosome: architecture and action of bacterial SMC and SMC-like complexes
URI https://onlinelibrary.wiley.com/doi/abs/10.1111%2F1574-6976.12045
https://www.ncbi.nlm.nih.gov/pubmed/24118085
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https://search.proquest.com/docview/1529947632
https://search.proquest.com/docview/1534096927
https://hal.science/hal-01893655
https://pubmed.ncbi.nlm.nih.gov/PMC4255302
Volume 38
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